ES2248819T3 - Peptidos anticongelantes de peces marinos como aditivos para productos alimentarios. - Google Patents
Peptidos anticongelantes de peces marinos como aditivos para productos alimentarios.Info
- Publication number
- ES2248819T3 ES2248819T3 ES96924879T ES96924879T ES2248819T3 ES 2248819 T3 ES2248819 T3 ES 2248819T3 ES 96924879 T ES96924879 T ES 96924879T ES 96924879 T ES96924879 T ES 96924879T ES 2248819 T3 ES2248819 T3 ES 2248819T3
- Authority
- ES
- Spain
- Prior art keywords
- polypeptide
- afp
- acid sequence
- hplc
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 133
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 104
- 239000000654 additive Substances 0.000 title claims abstract description 7
- 235000013305 food Nutrition 0.000 title claims description 56
- 229920001184 polypeptide Polymers 0.000 claims abstract description 92
- 150000001413 amino acids Chemical class 0.000 claims abstract description 68
- 230000000694 effects Effects 0.000 claims abstract description 64
- 238000000034 method Methods 0.000 claims abstract description 55
- 230000008569 process Effects 0.000 claims abstract description 9
- 230000000996 additive effect Effects 0.000 claims abstract description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 72
- 238000001953 recrystallisation Methods 0.000 claims description 34
- 108020004414 DNA Proteins 0.000 claims description 32
- 230000014509 gene expression Effects 0.000 claims description 28
- 150000007523 nucleic acids Chemical group 0.000 claims description 28
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 25
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 24
- 108010051210 beta-Fructofuranosidase Proteins 0.000 claims description 18
- 239000001573 invertase Substances 0.000 claims description 18
- 235000011073 invertase Nutrition 0.000 claims description 18
- 230000008878 coupling Effects 0.000 claims description 12
- 238000010168 coupling process Methods 0.000 claims description 12
- 238000005859 coupling reaction Methods 0.000 claims description 12
- 230000005764 inhibitory process Effects 0.000 claims description 11
- 239000000463 material Substances 0.000 claims description 9
- 102100039555 Galectin-7 Human genes 0.000 claims description 8
- 101000608772 Homo sapiens Galectin-7 Proteins 0.000 claims description 3
- 235000015243 ice cream Nutrition 0.000 claims description 3
- 230000001939 inductive effect Effects 0.000 claims description 3
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 claims description 2
- 235000012470 frozen dough Nutrition 0.000 claims description 2
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 22
- 235000012465 frozen bakery product Nutrition 0.000 claims 1
- 235000013611 frozen food Nutrition 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 66
- 102000004169 proteins and genes Human genes 0.000 abstract description 40
- 238000007710 freezing Methods 0.000 abstract description 21
- 230000008014 freezing Effects 0.000 abstract description 19
- 238000004128 high performance liquid chromatography Methods 0.000 abstract description 15
- 230000006872 improvement Effects 0.000 abstract description 10
- 230000002401 inhibitory effect Effects 0.000 abstract description 9
- 238000012986 modification Methods 0.000 abstract description 8
- 230000004048 modification Effects 0.000 abstract description 8
- 230000006378 damage Effects 0.000 abstract description 7
- 230000003405 preventing effect Effects 0.000 abstract description 5
- 241000269913 Pseudopleuronectes americanus Species 0.000 abstract 1
- 108010053481 Antifreeze Proteins Proteins 0.000 description 97
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 57
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 52
- 239000000047 product Substances 0.000 description 50
- 235000018102 proteins Nutrition 0.000 description 39
- 235000001014 amino acid Nutrition 0.000 description 31
- 229940024606 amino acid Drugs 0.000 description 31
- 101150047834 SNAI2 gene Proteins 0.000 description 29
- 239000013612 plasmid Substances 0.000 description 29
- 238000004519 manufacturing process Methods 0.000 description 27
- 108010029485 Protein Isoforms Proteins 0.000 description 26
- 102000001708 Protein Isoforms Human genes 0.000 description 26
- 230000002528 anti-freeze Effects 0.000 description 21
- 239000013078 crystal Substances 0.000 description 19
- 239000012634 fragment Substances 0.000 description 19
- 239000002904 solvent Substances 0.000 description 18
- 108020004705 Codon Proteins 0.000 description 16
- 241000269907 Pleuronectes platessa Species 0.000 description 15
- 241000251468 Actinopterygii Species 0.000 description 14
- 239000008280 blood Substances 0.000 description 13
- 210000004369 blood Anatomy 0.000 description 13
- 230000004927 fusion Effects 0.000 description 13
- 239000000203 mixture Substances 0.000 description 13
- 230000028327 secretion Effects 0.000 description 12
- 238000012360 testing method Methods 0.000 description 12
- 108091034117 Oligonucleotide Proteins 0.000 description 11
- 108700005078 Synthetic Genes Proteins 0.000 description 11
- 239000000243 solution Substances 0.000 description 11
- 241000588724 Escherichia coli Species 0.000 description 10
- 239000002609 medium Substances 0.000 description 10
- 238000004007 reversed phase HPLC Methods 0.000 description 10
- 241000894006 Bacteria Species 0.000 description 9
- 238000010276 construction Methods 0.000 description 9
- 230000029087 digestion Effects 0.000 description 9
- 239000000178 monomer Substances 0.000 description 9
- 230000009466 transformation Effects 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 238000000855 fermentation Methods 0.000 description 8
- 230000004151 fermentation Effects 0.000 description 8
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 8
- 239000006228 supernatant Substances 0.000 description 8
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 230000010354 integration Effects 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 230000002441 reversible effect Effects 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 241000196324 Embryophyta Species 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- SEQKRHFRPICQDD-UHFFFAOYSA-N N-tris(hydroxymethyl)methylglycine Chemical compound OCC(CO)(CO)[NH2+]CC([O-])=O SEQKRHFRPICQDD-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
- 238000004925 denaturation Methods 0.000 description 6
- 230000036425 denaturation Effects 0.000 description 6
- 101000887163 Gallus gallus Gallinacin-4 Proteins 0.000 description 5
- 101000887166 Gallus gallus Gallinacin-7 Proteins 0.000 description 5
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 239000007983 Tris buffer Substances 0.000 description 5
- 239000002253 acid Substances 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 239000012620 biological material Substances 0.000 description 5
- 229940041514 candida albicans extract Drugs 0.000 description 5
- 210000004027 cell Anatomy 0.000 description 5
- 239000008103 glucose Substances 0.000 description 5
- 238000009396 hybridization Methods 0.000 description 5
- 239000004615 ingredient Substances 0.000 description 5
- 230000032258 transport Effects 0.000 description 5
- 239000012138 yeast extract Substances 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 4
- 108020004511 Recombinant DNA Proteins 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
- 230000027455 binding Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 239000012153 distilled water Substances 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 239000004310 lactic acid Substances 0.000 description 4
- 235000014655 lactic acid Nutrition 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- 239000012901 Milli-Q water Substances 0.000 description 3
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 3
- 239000001888 Peptone Substances 0.000 description 3
- 108010080698 Peptones Proteins 0.000 description 3
- UZMAPBJVXOGOFT-UHFFFAOYSA-N Syringetin Natural products COC1=C(O)C(OC)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UZMAPBJVXOGOFT-UHFFFAOYSA-N 0.000 description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 3
- 239000004473 Threonine Substances 0.000 description 3
- 239000007997 Tricine buffer Substances 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- KCFYHBSOLOXZIF-UHFFFAOYSA-N dihydrochrysin Natural products COC1=C(O)C(OC)=CC(C2OC3=CC(O)=CC(O)=C3C(=O)C2)=C1 KCFYHBSOLOXZIF-UHFFFAOYSA-N 0.000 description 3
- 238000004520 electroporation Methods 0.000 description 3
- 229930182830 galactose Natural products 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 235000019319 peptone Nutrition 0.000 description 3
- 230000003248 secreting effect Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- 239000011782 vitamin Substances 0.000 description 3
- 235000013343 vitamin Nutrition 0.000 description 3
- 229940088594 vitamin Drugs 0.000 description 3
- 229930003231 vitamin Natural products 0.000 description 3
- 150000003722 vitamin derivatives Chemical class 0.000 description 3
- QZNNVYOVQUKYSC-JEDNCBNOSA-N (2s)-2-amino-3-(1h-imidazol-5-yl)propanoic acid;hydron;chloride Chemical compound Cl.OC(=O)[C@@H](N)CC1=CN=CN1 QZNNVYOVQUKYSC-JEDNCBNOSA-N 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 2
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 239000007984 Tris EDTA buffer Substances 0.000 description 2
- 241000269785 Zoarces americanus Species 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000005341 cation exchange Methods 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 235000013365 dairy product Nutrition 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 230000009746 freeze damage Effects 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 230000009036 growth inhibition Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 239000000700 radioactive tracer Substances 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 235000020183 skimmed milk Nutrition 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 239000013595 supernatant sample Substances 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 238000005084 2D-nuclear magnetic resonance Methods 0.000 description 1
- QRXMUCSWCMTJGU-UHFFFAOYSA-N 5-bromo-4-chloro-3-indolyl phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP(O)(=O)O)=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000186000 Bifidobacterium Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 230000008836 DNA modification Effects 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 241001625930 Luria Species 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 101100301239 Myxococcus xanthus recA1 gene Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- BTGMTHBOODBMHN-SUHMBNCMSA-N N-[3-[1-[[(3S)-2-hydroxy-5-oxooxolan-3-yl]carbamoyl]cyclopropyl]-2,4-dioxo-1-propan-2-ylpyrimidin-5-yl]-2-methyl-4-(naphthalen-2-ylamino)benzamide Chemical compound CC(C)n1cc(NC(=O)c2ccc(Nc3ccc4ccccc4c3)cc2C)c(=O)n(c1=O)C1(CC1)C(=O)N[C@H]1CC(=O)OC1O BTGMTHBOODBMHN-SUHMBNCMSA-N 0.000 description 1
- MQUQNUAYKLCRME-INIZCTEOSA-N N-tosyl-L-phenylalanyl chloromethyl ketone Chemical compound C1=CC(C)=CC=C1S(=O)(=O)N[C@H](C(=O)CCl)CC1=CC=CC=C1 MQUQNUAYKLCRME-INIZCTEOSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- BELBBZDIHDAJOR-UHFFFAOYSA-N Phenolsulfonephthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2S(=O)(=O)O1 BELBBZDIHDAJOR-UHFFFAOYSA-N 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 101000961042 Pseudopleuronectes americanus Ice-structuring protein A Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- PHMHDRYYFAYWEG-UHFFFAOYSA-N Rhapontigenin Natural products C1=C(O)C(OC)=CC=C1C=CC1=CC(O)=CC(O)=C1 PHMHDRYYFAYWEG-UHFFFAOYSA-N 0.000 description 1
- 108020001027 Ribosomal DNA Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 244000253911 Saccharomyces fragilis Species 0.000 description 1
- 235000018368 Saccharomyces fragilis Nutrition 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 101000582398 Staphylococcus aureus Replication initiation protein Proteins 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- YVNQAIFQFWTPLQ-UHFFFAOYSA-O [4-[[4-(4-ethoxyanilino)phenyl]-[4-[ethyl-[(3-sulfophenyl)methyl]amino]-2-methylphenyl]methylidene]-3-methylcyclohexa-2,5-dien-1-ylidene]-ethyl-[(3-sulfophenyl)methyl]azanium Chemical compound C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C(=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=2C(=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=C1 YVNQAIFQFWTPLQ-UHFFFAOYSA-O 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 101150055123 afp gene Proteins 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 150000003862 amino acid derivatives Chemical class 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 210000001557 animal structure Anatomy 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 235000015173 baked goods and baking mixes Nutrition 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 238000010261 blood fractionation Methods 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000012769 bulk production Methods 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000010411 cooking Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 239000013530 defoamer Substances 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 238000011143 downstream manufacturing Methods 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229960002885 histidine Drugs 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000007154 intracellular accumulation Effects 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- VIKNJXKGJWUCNN-XGXHKTLJSA-N norethisterone Chemical compound O=C1CC[C@@H]2[C@H]3CC[C@](C)([C@](CC4)(O)C#C)[C@@H]4[C@@H]3CCC2=C1 VIKNJXKGJWUCNN-XGXHKTLJSA-N 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 229960003531 phenolsulfonphthalein Drugs 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000037432 silent mutation Effects 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
- A23G9/00—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor
- A23G9/32—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds
- A23G9/38—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds containing peptides or proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/461—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from fish
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Inorganic Chemistry (AREA)
- Food Science & Technology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Polymers & Plastics (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Confectionery (AREA)
- Freezing, Cooling And Drying Of Foods (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Meat, Egg Or Seafood Products (AREA)
- General Preparation And Processing Of Foods (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP95201842 | 1995-07-05 | ||
| EP95201842 | 1995-07-05 | ||
| EP95202732 | 1995-10-10 | ||
| EP95202732 | 1995-10-10 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2248819T3 true ES2248819T3 (es) | 2006-03-16 |
Family
ID=26139472
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES05075582T Expired - Lifetime ES2420105T3 (es) | 1995-07-05 | 1996-07-01 | Expresión de péptidos anticongelantes de peces marinos en un organismo de calidad alimentaria y su aplicación en productos alimentarios |
| ES96924879T Expired - Lifetime ES2248819T3 (es) | 1995-07-05 | 1996-07-01 | Peptidos anticongelantes de peces marinos como aditivos para productos alimentarios. |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES05075582T Expired - Lifetime ES2420105T3 (es) | 1995-07-05 | 1996-07-01 | Expresión de péptidos anticongelantes de peces marinos en un organismo de calidad alimentaria y su aplicación en productos alimentarios |
Country Status (17)
| Country | Link |
|---|---|
| US (2) | US6914043B1 (ja) |
| EP (2) | EP1614753B1 (ja) |
| JP (2) | JP3926843B2 (ja) |
| CN (1) | CN1149285C (ja) |
| AT (1) | ATE305509T1 (ja) |
| AU (1) | AU723039B2 (ja) |
| BR (1) | BR9609325A (ja) |
| CA (1) | CA2226101C (ja) |
| CZ (1) | CZ698A3 (ja) |
| DE (1) | DE69635225T2 (ja) |
| DK (1) | DK0836646T3 (ja) |
| ES (2) | ES2420105T3 (ja) |
| HU (1) | HUP9802321A3 (ja) |
| PL (1) | PL324437A1 (ja) |
| SK (1) | SK179497A3 (ja) |
| TR (1) | TR199701752T1 (ja) |
| WO (1) | WO1997002343A1 (ja) |
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2315662A (en) * | 1996-07-26 | 1998-02-11 | Unilever Plc | Antifreeze peptides in frozen foods |
| PL331428A1 (en) * | 1996-07-26 | 1999-07-19 | Unilever Nv | Deep-frozen confectionery articles |
| GB2315661B (en) | 1996-07-26 | 2000-05-03 | Unilever Plc | Frozen food product |
| WO1998041109A1 (en) * | 1997-03-14 | 1998-09-24 | Unilever N.V. | Frozen food product containing anti-freeze peptides |
| DK0966206T3 (da) * | 1997-03-14 | 2005-07-25 | Unilever Nv | Frossent födevareprodukt indeholdende antifrysepeptider |
| WO1998041107A1 (en) * | 1997-03-14 | 1998-09-24 | Unilever N.V. | Frozen food product |
| GB9801410D0 (en) | 1998-01-22 | 1998-03-18 | Unilever Plc | Frozen food product |
| CA2363243C (en) * | 1999-03-10 | 2010-09-07 | Unilever Plc | Overrun water ice with antifreeze protein |
| GB9929696D0 (en) | 1999-12-15 | 2000-02-09 | Unilever Plc | Processes and organisms for the production of anti-freeze proteins |
| CN1481439A (zh) | 2000-12-13 | 2004-03-10 | 由真菌制备异源蛋白的方法 | |
| JP4228068B2 (ja) * | 2001-11-21 | 2009-02-25 | 独立行政法人産業技術総合研究所 | 魚類由来の不凍タンパク質 |
| BR0315943A (pt) * | 2002-12-20 | 2005-09-13 | Unilever Nv | Método para a produção de uma proteìna anticongelante e composição |
| US7098589B2 (en) | 2003-04-15 | 2006-08-29 | Luminus Devices, Inc. | Light emitting devices with high light collimation |
| JP2004344033A (ja) * | 2003-05-21 | 2004-12-09 | National Institute Of Advanced Industrial & Technology | 魚類が有する不凍タンパク質 |
| EP1541034A1 (en) * | 2003-12-10 | 2005-06-15 | Unilever Plc | Frozen confectionery product |
| EP1692163A1 (en) * | 2003-12-10 | 2006-08-23 | Unilever Plc | Frozen confectionery product comprising ice structuring proteins |
| ZA200800987B (en) * | 2005-09-23 | 2009-08-26 | Unilever Plc | Low pH aerated products |
| ZA200800988B (en) * | 2005-09-23 | 2009-08-26 | Unilever Plc | Aerated products with reduced creaming |
| EP1926399B2 (en) * | 2005-09-23 | 2014-03-12 | Unilever PLC | Process for producing a frozen aerated composition |
| DE602005006829D1 (de) | 2005-12-21 | 2008-06-26 | Unilever Nv | Gefrorene belüftete Süssspeisen |
| CA2617548C (en) * | 2006-01-31 | 2014-04-08 | Unilever Plc | Aerated compositions comprising hydrophobin |
| WO2007105734A1 (ja) | 2006-03-13 | 2007-09-20 | Nippon Suisan Kaisha, Ltd. | 不凍活性を有する甲殻類由来タンパク質 |
| ES2382100T3 (es) | 2006-10-20 | 2012-06-05 | Nestec S.A. | Péptidos estructurantes del hielo de origen láctico |
| BRPI0705417B1 (pt) * | 2006-12-20 | 2016-08-16 | Unilever Nv | produto alimentício aerado e processos para a produção de um produto alimentício aerado |
| US20100086662A1 (en) * | 2007-03-26 | 2010-04-08 | Andrew Richard Cox | Aerated food products being warm or having been heated up and methods for producing them |
| EP2129238A1 (en) * | 2007-03-26 | 2009-12-09 | Unilever N.V. | Aerated food products being warm containing soluble and/or insoluble solids and methods for producing them |
| BRPI0816506A2 (pt) * | 2007-10-18 | 2014-10-14 | Unilever Nv | "método para produzir um agente espumante" |
| WO2009065415A1 (en) | 2007-11-21 | 2009-05-28 | Roskilde Universitet | Polypeptides comprising an ice-binding activity |
| US20100112139A1 (en) * | 2008-03-28 | 2010-05-06 | Conopco, Inc., D/B/A Unilever | Foaming Agents Comprising Hydrophobin |
| AU2009304092B2 (en) * | 2008-10-16 | 2013-09-05 | Unilever Plc | Hydrophobin solution containing antifoam |
| CN102245628B (zh) * | 2008-12-16 | 2014-05-28 | 荷兰联合利华有限公司 | 从溶液中提取疏水蛋白的方法 |
| JP5681494B2 (ja) * | 2009-02-13 | 2015-03-11 | 株式会社カネカ | 氷結晶化阻害物質を含む植物抽出物およびその製造方法 |
| US8394444B2 (en) * | 2009-05-29 | 2013-03-12 | Conopco, Inc. | Oil-in-water emulsion |
| US8357420B2 (en) * | 2009-05-29 | 2013-01-22 | Conopco, Inc. | Oil-in-water emulsion |
| CA2704702C (en) * | 2009-06-02 | 2018-06-12 | Unilever Plc | Aerated baked products |
| US20110151064A1 (en) | 2009-12-21 | 2011-06-23 | Conopco, Inc., D/B/A Unilever | Particulate frozen confection |
| EP2347659B1 (en) | 2010-01-22 | 2012-08-22 | Unilever PLC | Process for producing frozen particles |
| JP2011229504A (ja) * | 2010-04-30 | 2011-11-17 | National Institute Of Advanced Industrial Science & Technology | 生産性および不凍活性を向上させた改変型不凍タンパク質とその製造方法 |
| EP2596706A4 (en) * | 2010-08-26 | 2015-01-28 | Nichirei Foods Inc | METHOD FOR INCREASING A HEAT HYSTERESIS ACTIVITY, METHOD FOR REDUCING THE THERMAL INACTIVATION OF A HEAT HYSTERESIS ACTIVITY AND COMPOSITION FOR INCREASING HEAT HYSTERESIS ACTIVITY |
| CN103648297B (zh) * | 2011-07-11 | 2016-10-05 | 荷兰联合利华有限公司 | 具有凝胶涂层的冷冻甜食 |
| US9513045B2 (en) | 2012-05-03 | 2016-12-06 | Whirlpool Corporation | Heater-less ice maker assembly with a twistable tray |
| US10426159B1 (en) | 2012-05-24 | 2019-10-01 | The Trustees Of California State University | Highly efficient enhancers for antifreeze protein activity |
| US8925335B2 (en) * | 2012-11-16 | 2015-01-06 | Whirlpool Corporation | Ice cube release and rapid freeze using fluid exchange apparatus and methods |
| US9476629B2 (en) | 2012-12-13 | 2016-10-25 | Whirlpool Corporation | Clear ice maker and method for forming clear ice |
| US9310115B2 (en) | 2012-12-13 | 2016-04-12 | Whirlpool Corporation | Layering of low thermal conductive material on metal tray |
| US9518773B2 (en) | 2012-12-13 | 2016-12-13 | Whirlpool Corporation | Clear ice maker |
| US9410723B2 (en) | 2012-12-13 | 2016-08-09 | Whirlpool Corporation | Ice maker with rocking cold plate |
| US9470448B2 (en) | 2012-12-13 | 2016-10-18 | Whirlpool Corporation | Apparatus to warm plastic side of mold |
| US9518770B2 (en) | 2012-12-13 | 2016-12-13 | Whirlpool Corporation | Multi-sheet spherical ice making |
| US9557087B2 (en) | 2012-12-13 | 2017-01-31 | Whirlpool Corporation | Clear ice making apparatus having an oscillation frequency and angle |
| US9500398B2 (en) | 2012-12-13 | 2016-11-22 | Whirlpool Corporation | Twist harvest ice geometry |
| US9273891B2 (en) | 2012-12-13 | 2016-03-01 | Whirlpool Corporation | Rotational ice maker |
| WO2014202089A2 (en) | 2013-06-18 | 2014-12-24 | Roskilde Universitet | Variants of anti-freeze polypeptides |
| DK3077517T3 (en) | 2013-12-02 | 2019-02-11 | Dsm Ip Assets Bv | ISSTRUCTURING PROTEIN |
| US9624418B2 (en) | 2014-04-15 | 2017-04-18 | Baker Hughes Incorporated | Antifreeze proteins for use in downhole fluids |
| WO2016065269A2 (en) | 2014-10-23 | 2016-04-28 | Whirlpool Corporation | Method and apparatus for increasing rate of ice production in an automatic ice maker |
| MX2017015126A (es) | 2015-06-02 | 2018-03-28 | Dsm Ip Assets Bv | Uso de proteina estructurante del hielo. |
| US11110176B2 (en) | 2016-11-25 | 2021-09-07 | The Board Of Trustees Of The California State University | Composition and method for the protection of proteins, cell components and cells during temperature stress |
| CN108118077A (zh) * | 2016-11-30 | 2018-06-05 | 中南大学 | 一种酶法水解三文鱼胶原制备抗氧化肽与抗冻肽的工艺 |
| CN107746870A (zh) * | 2017-10-26 | 2018-03-02 | 浙江海洋大学 | 一种金枪鱼鱼骨明胶抗冻肽及其制备方法 |
| US10739053B2 (en) | 2017-11-13 | 2020-08-11 | Whirlpool Corporation | Ice-making appliance |
| JP2021517143A (ja) * | 2018-03-14 | 2021-07-15 | バ、ヨン | Ｐｅｇ化不凍タンパク質およびそれを作製する方法およびそれを使用する方法 |
| US10907874B2 (en) | 2018-10-22 | 2021-02-02 | Whirlpool Corporation | Ice maker downspout |
| CN111808903B (zh) * | 2020-07-06 | 2023-03-31 | 浙江工业大学 | 一种安全高效蛋白抗冻剂及其制备方法和应用 |
| WO2024076237A1 (en) | 2022-10-06 | 2024-04-11 | Wageningen Universiteit | Improved ice-binding proteins based on twist constrained helices |
| CN116064709B (zh) * | 2022-11-02 | 2024-05-24 | 山东省海洋科学研究院(青岛国家海洋科学研究中心) | 一种天然抗冻肽及其制备方法和应用 |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5118792A (en) * | 1989-05-10 | 1992-06-02 | Dna Plant Technology Corporation | Ice crystal growth suppression polypeptides and method of making |
| US5849537A (en) * | 1989-09-19 | 1998-12-15 | Miller Brewing Company | Method of expressing antifreeze proteins in yeast |
| DE69129294T2 (de) * | 1990-01-17 | 1998-10-01 | The Regents Of The University Of California, Oakland, Calif. | Zusammensetzung zur verbesserung der lebenserhaltung biologischer materialien |
| WO1991012718A1 (en) * | 1990-03-01 | 1991-09-05 | Agouron Pharmaceuticals, Inc. | Enhanced cryopreservation with thermal hysteresis peptide |
| WO1994003617A1 (en) * | 1992-07-29 | 1994-02-17 | Unilever N.V. | Process for producing anti-freeze peptides |
| US5676985A (en) * | 1994-10-12 | 1997-10-14 | Hsc Research And Development Limited Partnership | Antifreeze polypeptide-expressing microorganisms useful in fermentation and freezing of foods |
| ATE287451T1 (de) | 1996-07-26 | 2005-02-15 | Unilever Nv | Gefrorenes lebensmittelprodukt das hitzestabiles gefrierschutzprotein enthält |
| GB2315661B (en) | 1996-07-26 | 2000-05-03 | Unilever Plc | Frozen food product |
| PL331428A1 (en) | 1996-07-26 | 1999-07-19 | Unilever Nv | Deep-frozen confectionery articles |
| CA2363243C (en) | 1999-03-10 | 2010-09-07 | Unilever Plc | Overrun water ice with antifreeze protein |
| GB9929696D0 (en) * | 1999-12-15 | 2000-02-09 | Unilever Plc | Processes and organisms for the production of anti-freeze proteins |
| BR112014004817A2 (pt) | 2011-08-29 | 2017-05-30 | Crow Equipment Corp | sistema para prover uma interface de controle de navegação veicular, e, veículo |
-
1996
- 1996-07-01 AU AU65190/96A patent/AU723039B2/en not_active Ceased
- 1996-07-01 CA CA002226101A patent/CA2226101C/en not_active Expired - Fee Related
- 1996-07-01 DE DE69635225T patent/DE69635225T2/de not_active Expired - Lifetime
- 1996-07-01 ES ES05075582T patent/ES2420105T3/es not_active Expired - Lifetime
- 1996-07-01 PL PL96324437A patent/PL324437A1/xx unknown
- 1996-07-01 HU HU9802321A patent/HUP9802321A3/hu unknown
- 1996-07-01 CN CNB961965010A patent/CN1149285C/zh not_active Expired - Fee Related
- 1996-07-01 EP EP05075582.6A patent/EP1614753B1/en not_active Expired - Lifetime
- 1996-07-01 AT AT96924879T patent/ATE305509T1/de not_active IP Right Cessation
- 1996-07-01 JP JP50482897A patent/JP3926843B2/ja not_active Expired - Fee Related
- 1996-07-01 CZ CZ986A patent/CZ698A3/cs unknown
- 1996-07-01 SK SK1794-97A patent/SK179497A3/sk unknown
- 1996-07-01 WO PCT/EP1996/002936 patent/WO1997002343A1/en active IP Right Grant
- 1996-07-01 EP EP96924879A patent/EP0836646B1/en not_active Expired - Lifetime
- 1996-07-01 ES ES96924879T patent/ES2248819T3/es not_active Expired - Lifetime
- 1996-07-01 DK DK96924879T patent/DK0836646T3/da active
- 1996-07-01 BR BR9609325A patent/BR9609325A/pt not_active Application Discontinuation
- 1996-07-01 TR TR97/01752T patent/TR199701752T1/xx unknown
- 1996-07-02 US US08/673,876 patent/US6914043B1/en not_active Expired - Fee Related
-
2003
- 2003-08-08 JP JP2003290511A patent/JP3921461B2/ja not_active Expired - Fee Related
-
2004
- 2004-09-03 US US10/934,009 patent/US7297516B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| ES2420105T3 (es) | 2013-08-22 |
| EP1614753B1 (en) | 2013-05-29 |
| JP3921461B2 (ja) | 2007-05-30 |
| SK179497A3 (en) | 1998-07-08 |
| WO1997002343A1 (en) | 1997-01-23 |
| US20050205833A1 (en) | 2005-09-22 |
| CA2226101C (en) | 2009-06-23 |
| CZ698A3 (cs) | 1998-05-13 |
| JPH11508451A (ja) | 1999-07-27 |
| HUP9802321A3 (en) | 2000-10-30 |
| EP1614753A2 (en) | 2006-01-11 |
| EP0836646A1 (en) | 1998-04-22 |
| DE69635225D1 (de) | 2006-02-09 |
| AU723039B2 (en) | 2000-08-17 |
| US6914043B1 (en) | 2005-07-05 |
| JP3926843B2 (ja) | 2007-06-06 |
| TR199701752T1 (xx) | 1998-05-21 |
| EP1614753A3 (en) | 2006-07-19 |
| DK0836646T3 (da) | 2005-12-19 |
| BR9609325A (pt) | 1999-05-25 |
| CN1193999A (zh) | 1998-09-23 |
| EP0836646B1 (en) | 2005-09-28 |
| AU6519096A (en) | 1997-02-05 |
| PL324437A1 (en) | 1998-05-25 |
| ATE305509T1 (de) | 2005-10-15 |
| HUP9802321A2 (hu) | 1999-02-01 |
| CN1149285C (zh) | 2004-05-12 |
| MX9800016A (es) | 1998-07-31 |
| JP2004043484A (ja) | 2004-02-12 |
| US7297516B2 (en) | 2007-11-20 |
| CA2226101A1 (en) | 1997-01-23 |
| DE69635225T2 (de) | 2006-03-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2248819T3 (es) | Peptidos anticongelantes de peces marinos como aditivos para productos alimentarios. | |
| CN101918437B (zh) | 具有冰结合活性的多肽 | |
| Zendo et al. | Identification of the lantibiotic nisin Q, a new natural nisin variant produced by Lactococcus lactis 61-14 isolated from a river in Japan | |
| Yuan et al. | Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants | |
| Maqueda et al. | Peptide AS-48: prototype of a new class of cyclic bacteriocins | |
| ES2291021T3 (es) | Gen codificando para la heliomicina y su utilizacion. | |
| Harris et al. | Anionic antimicrobial peptides from eukaryotic organisms and their mechanisms of action | |
| ES2312441T3 (es) | Bacteriocina anti-listeria. | |
| JP3474200B2 (ja) | ニンジン抗凍結ポリペプチド | |
| Akca et al. | Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci | |
| AU2001246533B2 (en) | Anti-freeze proteins, their production and use | |
| AU7973700A (en) | Lantibiotic | |
| PT95666B (pt) | Processo para a preparacao de aditivos para alimentos | |
| Simons et al. | Overproduction of bovine β-casein in Escherichia coli and engineering of its main chymosin cleavage site | |
| US20070276124A1 (en) | Protein Expression | |
| MXPA98000016A (en) | Expression of ocean fish antifreeze peptide in a food grade organism and its application in alimentic products | |
| ES2247872B1 (es) | Pepsina y pepsinogeno bovinos recombinantes producidos en celulas procariotas y eucariotas. | |
| WO1994004682A1 (en) | Bacteriocin | |
| Veeraragavan | Studies on two major contaminating proteins of the cytoplasmic inclusion bodies in Escherichia coli | |
| ES2349072T3 (es) | Lactobacilus de una bacteriocina anti-listeria. | |
| CN101665533A (zh) | 蛋白质活性多肽及其编码基因、表达载体、表达菌及应用 | |
| Alpert et al. | Molecular Cloning and DNA Sequence of ZucE, the Gene Encoding the Lactose-specific Enzyme II of the Phosphotransferase System of | |
| JPH07196688A (ja) | 新規な生理活性ポリペプチド、その製造方法及び用途 | |
| HU217102B (hu) | Tisztított neurotróf faktor és eljárás előállítására |